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Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell types have...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

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Updated: May 9, 2026

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

Membrane protein structure determination - the next generation.

Isabel Moraes1, Gwyndaf Evans, Juan Sanchez-Weatherby

  • 1Department of Life Sciences, Imperial College London, London SW7 2AZ, UK; Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK; Research Complex at Harwell Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK.

Biochimica Et Biophysica Acta
|July 18, 2013
PubMed
Summary
This summary is machine-generated.

Determining membrane protein structures using X-ray crystallography is challenging due to crystal growth limitations. This review highlights innovative methods and synchrotron strategies to overcome these bottlenecks for drug discovery.

Keywords:
Crystal dehydrationCrystal seedingIn situ data collectionMacromolecular crystallographyMembrane proteinXFEL

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

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Last Updated: May 9, 2026

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

Area of Science:

  • Membrane Protein Structural Biology
  • Biochemistry
  • Drug Discovery

Background:

  • Significant advancements in membrane protein structural biology since 1985.
  • Over 350 unique membrane protein structures are available in the Protein Data Bank.
  • High-throughput technologies and genomics/proteomics have accelerated structure determination.

Purpose of the Study:

  • To review the latest methods and strategies for producing suitable membrane protein crystals.
  • To highlight the impact of third-generation synchrotron radiation in the field.
  • To summarize synchrotron beamline strategies for screening and data collection.

Main Methods:

  • X-ray crystallography for atomic resolution structure determination.
  • Innovative approaches for membrane protein crystallization.
  • Utilizing third-generation synchrotron radiation for data collection.

Main Results:

  • X-ray crystallography remains crucial for understanding protein-ligand interactions.
  • Membrane protein crystal growth is a significant bottleneck.
  • Advanced synchrotron techniques improve data collection from challenging crystals.

Conclusions:

  • Innovative crystallization methods are essential for membrane protein structure determination.
  • Third-generation synchrotrons significantly aid in analyzing demanding crystals.
  • Overcoming crystallization challenges is key for advancing membrane protein research and drug discovery.